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The filovirus glycoprotein (GP) is the sole surface protein of filoviruses, including Ebola and Marburg viruses. It is essential for viral attachment, entry into host cells, and membrane fusion. The GP exists as a homotrimer on the viral envelope; each monomer consists of two subunits—GP1 and GP2—linked by a disulfide bond. GP1 contains the receptor-binding site (RBS), glycan cap, and mucin-like domain. Responsible for initial attachment to host cell receptors or attachment factors such as C-type lectins. GP2 contains heptad repeat regions, fusion loop, and transmembrane domain. Mediates membrane fusion between virus and host cell after conformational changes triggered in endosomes. Highly glycosylated with both N-linked and O-linked glycans concentrated in the mucin-like region (MLR), which plays roles in immune evasion and cell tropism.
Inhibition of viral attachment, entry, or membrane fusion
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